Pyruvate-ferredoxin oxidoreductase

spinqualitylabelsall models Pyruvate-ferredoxin oxidoredoxin dimer with Fe4S4 cluster complex with thiamine diphosphate and pyruvate 2c3o Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Pyruvate-ferredoxin oxidoreductase (PFOR) is an enzyme of the fermentation cycle which catalyzes the oxidative decarboxylation of pyruvate to acetyl CoA and CO2. This reaction provides the electron source for the reduction of ferredoxin. The reaction is CoA-dependent and contains thiamine diphosphate (TDP). PFOR contains iron-sulfur clusters (Fe4S4). Structural highlights The active site of PFOR contains thiamine diphosphate and pyruvate. Mg coordination site. Water molecules are shown as red spheres. Fe4S4 cluster interactions. Each Fe atom interacts with S atom from cysteine.

3D structures of pyruvate-ferredoxin oxidoreductase

04-October-2023

1b0p, 2c3m – DaPFOR + TDP – Desulfovibrio africanus
2pda, 2c3o, 2c42 - DaPFOR + pyruvate + TDP
1kek, 2c3y, 2uza - DaPFOR + CO2 + acetyl-TDP
2c3p - DaPFOR + TDP derivative
2c3u - DaPFOR + pyruvate + TDP derivative
7plm – DaPFOR + TPP – Cryo EM
2raa - PFOR γ subunit - Thermotoga maritima
6cin – MtPFOR + TDP – Moorella thermoacetica
6cio, 6cip – MtPFOR + TTP derivative
6ciq – MtPFOR + TTP + CoA

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky